Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Basic phospholipase A2 vipoxin B chain

Gene
N/A
Organism
Vipera ammodytes meridionalis (Eastern sand viper)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterodimer: postsynaptic neurotoxin.
Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Calcium; via carbonyl oxygenBy similarity
Metal bindingi29 – 291Calcium; via carbonyl oxygenBy similarity
Metal bindingi31 – 311Calcium; via carbonyl oxygenBy similarity
Active sitei47 – 4711 Publication
Metal bindingi48 – 481CalciumBy similarity
Active sitei89 – 8911 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemostasis impairing toxin, Hydrolase, Neurotoxin, Platelet aggregation inhibiting toxin, Postsynaptic neurotoxin, Toxin

Keywords - Biological processi

Cytolysis, Hemolysis, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 vipoxin B chain (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Vipoxin toxic component
OrganismiVipera ammodytes meridionalis (Eastern sand viper)
Taxonomic identifieri73841 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of the heterodimer is 0.7-1.2 mg/kg by intraperitoneal injection into mice and 0.9-1.3 mg/kg by intravenous injection into mice.1 Publication
LD50 of the basic component is 10-13 mg/kg by intraperitoneal injection into mice, and 2.2-3.0 mg/kg by intravenous injection into mice, corresponding to 2.4-fold and more than 10-fold the LD50 of the heterodimer, respectively.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Basic phospholipase A2 vipoxin B chainPRO_0000161712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 115Combined sources2 Publications
Disulfide bondi28 ↔ 44Combined sources2 Publications
Disulfide bondi43 ↔ 95Combined sources2 Publications
Disulfide bondi49 ↔ 122Combined sources2 Publications
Disulfide bondi50 ↔ 88Combined sources2 Publications
Disulfide bondi57 ↔ 81Combined sources2 Publications
Disulfide bondi75 ↔ 86Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of A (AC P04084) and B chains; non-covalently linked. The A chain (acidic) is non-toxic, and increases the toxicity of the B chain (basic). The A chain may act as factor stabilizing the complex structure and hence retaining its toxicity by preventing non-specific binding. Upon binding to the target membranes the A chain is postulated to dissociate.3 Publications

Protein-protein interaction databases

MINTiMINT-220273.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Helixi17 – 215Combined sources
Beta strandi22 – 243Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 303Combined sources
Helixi39 – 5214Combined sources
Turni59 – 613Combined sources
Beta strandi66 – 694Combined sources
Beta strandi72 – 754Combined sources
Helixi81 – 9818Combined sources
Helixi100 – 1023Combined sources
Helixi105 – 1073Combined sources
Helixi112 – 1154Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00B1-122[»]
1JLTX-ray1.40B1-122[»]
1RGBX-ray3.30A/B/K/L1-112[»]
ProteinModelPortaliP14420.
SMRiP14420. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14420.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NLFQFAKMIN GKLGAFSVWN YISYGCYCGW GGQGTPKDAT DRCCFVHDCC
60 70 80 90 100
YGRVRGCNPK LAIYSYSFKK GNIVCGKNNG CLRDICECDR VAANCFHQNK
110 120
NTYNKNYKFL SSSRCRQTSE QC
Length:122
Mass (Da):13,828
Last modified:January 1, 1990 - v1
Checksum:i94438F9F1285FC7D
GO

Sequence databases

PIRiA29290.

Cross-referencesi

Sequence databases

PIRiA29290.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00B1-122[»]
1JLTX-ray1.40B1-122[»]
1RGBX-ray3.30A/B/K/L1-112[»]
ProteinModelPortaliP14420.
SMRiP14420. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-220273.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP14420.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes)."
    Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G.
    Biol. Chem. Hoppe-Seyler 368:343-352(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: Bulgarian.
    Tissue: Venom.
  2. "Acute toxicity of vipoxin and its components: is the acidic component an 'inhibitor' of PLA2 toxicity?"
    Atanasov V.N., Stoykova S., Goranova Y., Mitewa M., Petrova S.
    Interdiscip. Toxicol. 5:169-172(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, LETHAL DOSES.
    Tissue: Venom.
  3. "Hemolytic activity and platelet aggregation inhibitory effect of vipoxin's basic sPLA2 subunit."
    Stoykova S., Goranova Y., Pantcheva I., Atanasov V., Danchev D., Petrova S.
    Interdiscip. Toxicol. 6:136-140(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE MONOMER.
  4. "Crystals of phospholipase A2 inhibitor. The non-toxic component of vipoxin from the venom of Bulgarian viper (Vipera ammodytes)."
    Devedjiev Y., Atanasov B., Mancheva I., Aleksiev B.
    J. Mol. Biol. 229:1147-1149(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Tissue: Venom.
  5. "Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor."
    Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B., Singh T.P.
    J. Mol. Biol. 231:498-500(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    Tissue: Venom.
  6. "Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution."
    Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B., Genov N., Willingmann P., Weber W., Singh T.P., Betzel C.
    FEBS Lett. 412:573-577(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH VIPOXIN A CHAIN, DISULFIDE BONDS.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH VIPOXIN A CHAIN, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2B_VIPAE
AccessioniPrimary (citable) accession number: P14420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

The B chain (not complexed with the A chain) does not induce neurotoxic symptoms, hemorrhage, organ injuries and other macroscopic changes.1 Publication

Caution

The acidic chain was originally postulated to act as an inhibitor of the basic chain.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.